abbreviation officialName equation geneAssociation ecocyc-rxn-ids analysis notes
2AGPE120tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C12:0 ) transporter via facilitated diffusion ( periplasm ) 2agpe120[p] --> 2agpe120[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPE140tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C14:0 ) transporter via facilitated diffusion ( periplasm ) 2agpe140[p] --> 2agpe140[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPE141tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C14:1 ) transporter via facilitated diffusion ( periplasm ) 2agpe141[p] --> 2agpe141[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPE160tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C16:0 ) transporter via facilitated diffusion ( periplasm ) 2agpe160[p] --> 2agpe160[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPE161tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C16:1 ) transporter via facilitated diffusion ( periplasm ) 2agpe161[p] --> 2agpe161[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPE180tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C18:0 ) transporter via facilitated diffusion ( periplasm ) 2agpe180[p] --> 2agpe180[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPE181tipp 2-Acyl-sn-glycero-3-phosphoethanolamine ( n-C18:1 ) transporter via facilitated diffusion ( periplasm ) 2agpe181[p] --> 2agpe181[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPG160tipp 2-Acyl-sn-glycero-3-phosphoglycerol ( n-C16:0 ) transporter via facilitated diffusion ( periplasm ) 2agpg160[p] --> 2agpg160[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
2AGPG161tipp 2-Acyl-sn-glycero-3-phosphoglycerol ( n-C16:1 ) transporter via facilitated diffusion ( periplasm ) 2agpg161[p] --> 2agpg161[c] B2835 B2835 : (LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of lysophospholipids. Mutation experiments and transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas gene |CITS:[15661733]|.)
ACACt2pp acetoacetate transport via proton symport ( periplasm ) acac[p] + h[p] <==> acac[c] + h[c] B2223 B2223 : (No information about this protein was found by a literature search conducted on June 13, 2005. )
ADNtex adenosine transport via diffusion ( extracellular to periplasm ) adn[e] <==> adn[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
ALLTNt2rpp allantoin transport in via proton symport ( periplasm ) alltn[p] + h[p] <==> alltn[c] + h[c] B0511 B0511 : (The YbbW protein is an uncharacterized member of the NCS1 family of purine and pyrimidine transporters |CITS: [99184734]|. Based on sequence similarity, YbbW may function as a proton-driven allantoin uptake system. Supporting this notion, the downstream gene from ybbW encodes a putative allantoinase enzyme.)
ALPATE160pp "apolipoprotein N-acyltransferase ( phosphatidylethanolamine, periplasm )" [p] : alpp + pe160 --> 2agpe160 + lpp ( B0657 AND B1677 ) B0657 : (Apolipoprotein N-acyltransferase activity transfers palmitate to apolipoproteins, resulting in the maturation of lipoproteins from apolipoprotein precursors |CITS: [2032623]|. Aminoacylation of lipoproteins bound for the outer membrane is required for proper localization of these lipoproteins via the Lol pathway |CITS: [12198129]|. The enzyme activity has been characterized |CITS: [2032623]|. The enzyme can utilize the phospholipids phosphatidylethanolamine, phosphatidylglycerol, or cardiolipin in vitro |CITS: [2032623]|. A pss mutant exhibits apolipoprotein N-acyltransferase activity, indicating that the enzyme is not specific for a phosphatidylethanolamine donor in vivo |CITS: [2033085]|. Apolipoprotein N-acyltransferase localizes to inner membrane or inner-plus-outer membrane fractions |CITS: [2032623]|. A cutE mutant exhibits copper sensitivity |CITS: [1938881]|. CutE has a region with similarity to copper binding sites |CITS: [1938881]|. CutE functionally complements the heat sensitivity, copper sensitivity, and apolipoprotein N-acyltransferase defect of a Salmonella typhimurium SE5312 mutant |CITS: [8344936]|. CutE overproduction in Salmonella typhimurium results in increased apolipoprotein N-acyltransferase activity |CITS: [8344936]|. CutE has similarity to Rhizobium meliloti ActA |CITS: [8868435]|. Regulation has been described |CITS: [1938881]|. Review: |CITS: [7651187]|.) B1677 : (Lpp, the major lipoprotein, is one of the most abundant proteins in Escherichia coli |CITS:[4610570]| and is necessary for the stabilization and integrity of the bacterial cell envelope |CITS:[11790745]|. The three-dimensional crystal structure of Lpp has been determined to 1.9 A resolution |CITS:[10843861]|. Cells lacking Lpp or with mutations affecting the attachment of Lpp to the murein (peptidoglycan) layer exhibit outer membrane blebs, are hypersensitive to toxic compounds, and release periplasmic proteins to the extracellular medium |CITS:[105245]|. Lpp exists in two forms, a free form and a covalently linked bound form attached to the peptidoglycan. Both forms are localized to the outer membrane |CITS:[4245367]|, |CITS:[4565677]|. Lpp is expressed as a prolipoprotein, having 20 amino acid residues extending from the amino terminus |CITS:[322142]| During translocation across the cytoplasmic membrane, the prolipoprotein undergoes modifications of the amino terminus cysteine residue followed by cleavage of the signal peptide extension |CITS:[8051048]|. The mature lipoprotein is then translocated to the outer membrane where it is covalently bound to the peptidoglycan layer |CITS:[6369111]|, |CITS:[6363408]|. Globomycin was found to inhibit the cleavage by signal peptidase II through noncompetitive binding to the enzyme |CITS:[3888977]|. Studies using inhibitors of the proton motive force (pmf) and ATP-depleted cells indicated that both the pmf and ATP are required for translocation of an OmpF-Lpp chimeric protein |CITS:[3029075]|. Translocation across the inner membrane was found to involve the Sec export apparatus |CITS:[2842297]|. Immunoelectron microscopy revealed that free lipoprotein is inserted equally over the entire cell wall, that lipoprotein synthesis increases with cell length, and that cell shape depends on total lipoprotein content of the cell in that low total lipoprotein corresponds to a spherical shape and a higher lipoprotein content corresponds with a rod shape |CITS:[3316185]|. Pulse-chase labeling followed by cell fractionation found that Lpp utilizes the LolA-LolB system to facilitate its release from the inner membrane and localization to the outer membrane |CITS:[10521496]|. Chemical cross-linking has revealed that Lpp organizes into trimers and interacts with OmpA, a major outer membrane lipoprotein |CITS:[3013869]|.)
ALPATG160pp "apolipoprotein N-acyltransferase ( phosphatidylglycerol, periplasm )" [p] : alpp + pg160 --> 2agpg160 + lpp ( B0657 AND B1677 ) B0657 : (Apolipoprotein N-acyltransferase activity transfers palmitate to apolipoproteins, resulting in the maturation of lipoproteins from apolipoprotein precursors |CITS: [2032623]|. Aminoacylation of lipoproteins bound for the outer membrane is required for proper localization of these lipoproteins via the Lol pathway |CITS: [12198129]|. The enzyme activity has been characterized |CITS: [2032623]|. The enzyme can utilize the phospholipids phosphatidylethanolamine, phosphatidylglycerol, or cardiolipin in vitro |CITS: [2032623]|. A pss mutant exhibits apolipoprotein N-acyltransferase activity, indicating that the enzyme is not specific for a phosphatidylethanolamine donor in vivo |CITS: [2033085]|. Apolipoprotein N-acyltransferase localizes to inner membrane or inner-plus-outer membrane fractions |CITS: [2032623]|. A cutE mutant exhibits copper sensitivity |CITS: [1938881]|. CutE has a region with similarity to copper binding sites |CITS: [1938881]|. CutE functionally complements the heat sensitivity, copper sensitivity, and apolipoprotein N-acyltransferase defect of a Salmonella typhimurium SE5312 mutant |CITS: [8344936]|. CutE overproduction in Salmonella typhimurium results in increased apolipoprotein N-acyltransferase activity |CITS: [8344936]|. CutE has similarity to Rhizobium meliloti ActA |CITS: [8868435]|. Regulation has been described |CITS: [1938881]|. Review: |CITS: [7651187]|.) B1677 : (Lpp, the major lipoprotein, is one of the most abundant proteins in Escherichia coli |CITS:[4610570]| and is necessary for the stabilization and integrity of the bacterial cell envelope |CITS:[11790745]|. The three-dimensional crystal structure of Lpp has been determined to 1.9 A resolution |CITS:[10843861]|. Cells lacking Lpp or with mutations affecting the attachment of Lpp to the murein (peptidoglycan) layer exhibit outer membrane blebs, are hypersensitive to toxic compounds, and release periplasmic proteins to the extracellular medium |CITS:[105245]|. Lpp exists in two forms, a free form and a covalently linked bound form attached to the peptidoglycan. Both forms are localized to the outer membrane |CITS:[4245367]|, |CITS:[4565677]|. Lpp is expressed as a prolipoprotein, having 20 amino acid residues extending from the amino terminus |CITS:[322142]| During translocation across the cytoplasmic membrane, the prolipoprotein undergoes modifications of the amino terminus cysteine residue followed by cleavage of the signal peptide extension |CITS:[8051048]|. The mature lipoprotein is then translocated to the outer membrane where it is covalently bound to the peptidoglycan layer |CITS:[6369111]|, |CITS:[6363408]|. Globomycin was found to inhibit the cleavage by signal peptidase II through noncompetitive binding to the enzyme |CITS:[3888977]|. Studies using inhibitors of the proton motive force (pmf) and ATP-depleted cells indicated that both the pmf and ATP are required for translocation of an OmpF-Lpp chimeric protein |CITS:[3029075]|. Translocation across the inner membrane was found to involve the Sec export apparatus |CITS:[2842297]|. Immunoelectron microscopy revealed that free lipoprotein is inserted equally over the entire cell wall, that lipoprotein synthesis increases with cell length, and that cell shape depends on total lipoprotein content of the cell in that low total lipoprotein corresponds to a spherical shape and a higher lipoprotein content corresponds with a rod shape |CITS:[3316185]|. Pulse-chase labeling followed by cell fractionation found that Lpp utilizes the LolA-LolB system to facilitate its release from the inner membrane and localization to the outer membrane |CITS:[10521496]|. Chemical cross-linking has revealed that Lpp organizes into trimers and interacts with OmpA, a major outer membrane lipoprotein |CITS:[3013869]|.)
ARGORNt7pp arginine/ornithine antiporter ( periplasm ) arg-L[p] + orn[c] <==> arg-L[c] + orn[p] B1605 B1605 : (ArcD is an uncharacterised member of the APC family of amino acid transporters. ArcD is highly similar to the Pseudomonas aeruginosa ArcD arginine/ornithine antiporter and probably has a similar function.)
ARGt3pp L-arginine transport out via proton antiport ( cytoplasm to periplasm ) arg-L[c] + h[p] --> arg-L[p] + h[c] B2923 B2923 : (The ArgO (YggA) protein is a member of the LysE family of lysine efflux transporters |CITS: [99257453]|. Based on sequence similarity, ArgO may function as a proton-driven amino acid efflux system. Null mutations in both the argO and the argP genes cause hypersensitivity to canavanine, an arginine analog. ArgO expression is regulated by ArgP, and transcription of argO is induced by exogenous arginine |CITS: [15150242]|. ArgO = "arginine outward transport" |CITS: [15150242]|)
ASCBPL L-ascorbate 6-phosphate lactonase [c] : ascb6p + h2o --> 3dhgulnp + h B4192 B4192 : (UlaG is required for the ability to utilize L-ascorbate as the sole carbon source under anaerobic growth conditions |CITS: [12644495]|. The enzyme was suggested to be a cytoplasmic L-ascorbate 6-phosphate lactonase |CITS: [12644495]|. Phosphodiesterase activity of UlaG was discovered in a high-throughput screen of purified proteins |CITS: [15808744]|. Expression of ulaG is negatively regulated by UlaR |CITS: [12374842]|.)
BUTt2rpp "Butyrate transport via proton symport, reversible ( periplasm )" but[p] + h[p] <==> but[c] + h[c] B2223 B2223 : (No information about this protein was found by a literature search conducted on June 13, 2005. )
CD2abcpp Cadmium ( Cd+2 ) ABC transporter ( periplasm ) atp[c] + cd2[c] + h2o[c] --> adp[c] + cd2[p] + h[c] + pi[c] B3469 B3469 : (The gene product of the yhhO gene, also referred to as zntA, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|. ZntA displays a Km of approximately 20 μM for Cd(II) and 100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|. A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|. The zntA gene was found to be under the control of the transcriptional regulator ZntR. zntA expression is activated by an increased concentration of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by Zn(II) |CITS:[20127859]|.)
CHLabcpp choline transport via ABC system ( periplasm ) atp[c] + chol[p] + h2o[c] --> adp[c] + chol[c] + h[c] + pi[c] ( B2128 AND B2129 AND B2130 AND B2131 ) B2128 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.) B2129 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.) B2130 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.) B2131 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.)
COBALT2abcpp Cobalt ( Co+2 ) ABC transporter ( periplasm ) atp[c] + cobalt2[c] + h2o[c] --> adp[c] + cobalt2[p] + h[c] + pi[c] B3469 B3469 : (The gene product of the yhhO gene, also referred to as zntA, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|. ZntA displays a Km of approximately 20 μM for Cd(II) and 100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|. A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|. The zntA gene was found to be under the control of the transcriptional regulator ZntR. zntA expression is activated by an increased concentration of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by Zn(II) |CITS:[20127859]|.)
CU1abcpp Copper ( Cu +1 ) ABC transporter ( periplasm ) atp[c] + cu[c] + h2o[c] --> adp[c] + cu[p] + h[c] + pi[c] B0484 B0484 : (YbaR is an uncharacterized member of the P-type ATPase cation transporter family |CITS:[94202222]|. Based on sequence similarity, it may function as a copper transporting ATPase.)
CU2abcpp Copper ( Cu+2 ) ABC transporter ( periplasm ) atp[c] + cu2[c] + h2o[c] --> adp[c] + cu2[p] + h[c] + pi[c] B3469 B3469 : (The gene product of the yhhO gene, also referred to as zntA, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|. ZntA displays a Km of approximately 20 μM for Cd(II) and 100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|. A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|. The zntA gene was found to be under the control of the transcriptional regulator ZntR. zntA expression is activated by an increased concentration of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by Zn(II) |CITS:[20127859]|.)
DADNtex deoxyadenosine transport via diffusion ( extracellular to periplasm ) dad-2[e] <==> dad-2[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
DCYTtex deoxycytidine transport via diffusion ( extracellular to periplasm ) dcyt[e] <==> dcyt[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
DURItex deoxyuridine transport via diffusion ( extracellular to periplasm ) duri[e] <==> duri[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
ECAtpp "enterobacterial common antigen transferase ( flippase, cytoplasm to periplasm )" unagamuf[c] --> unagamuf[p] B3792 B3792 : (The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)
FRULYSt2pp Fructoselysine transport via proton symport ( periplasm ) frulys[p] + h[p] --> frulys[c] + h[c] B3370 B3370 : (FrlA is an uncharacterized member of the APC superfamily of amino acid transporters |CITS:[20391827]|. Based on the activities of FrlB and FrlD, FrlA is suggested to transport fructoselysine, which can be utilized as a carbon source |CITS: [12147680]|. The function of FrlA has not been experimentally determined. An frlA mutant is unable to grow on 20mM fructoselysine or psicoselysine as the sole source of carbon |CITS: [14641112]|. FrlA: "fructoselysine" |CITS: [12147680]|.)
GALCTt2rpp "D-galactarte transport via proton symport, reversible ( periplasm )" galct-D[p] + h[p] <==> galct-D[c] + h[c] ( B2789 OR B3127 ) B2789 : (The YgcZ protein may function as a glucarate transporter. The ygcZ gene is encoded in a probable operon with genes encoding two subunits of a putative glucarate dehydratase. YgcZ is a member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]| and shares a high level of sequence similarity with probable glucarate transporters from various organisms. YgcZ probably functions as a glucarate/proton transporter.) B3127 : (YhaU is an uncharacterised member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]|. Based on sequence similarity, YhaU may function as a proton-driven glucarate uptake system.)
GLCRt2rpp "D-glucarate transport via proton symport, reversible ( periplasm )" glcr[p] + h[p] <==> glcr[c] + h[c] ( B3127 OR B2789 ) B2789 : (The YgcZ protein may function as a glucarate transporter. The ygcZ gene is encoded in a probable operon with genes encoding two subunits of a putative glucarate dehydratase. YgcZ is a member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]| and shares a high level of sequence similarity with probable glucarate transporters from various organisms. YgcZ probably functions as a glucarate/proton transporter.) B3127 : (YhaU is an uncharacterised member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]|. Based on sequence similarity, YhaU may function as a proton-driven glucarate uptake system.)
GLYBabcpp Glycine betaine transport via ABC system ( periplasm ) atp[c] + glyb[p] + h2o[c] --> adp[c] + glyb[c] + h[c] + pi[c] ( B2128 AND B2129 AND B2130 AND B2131 ) B2128 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.) B2129 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.) B2130 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.) B2131 : (YehX, YehW, YehY, YehZ are uncharacterized members of the ABC superfamily of transporters |CITS: [99091701]|. YehX is the putative ATP binding component, YehW and YehY are the membrane components, and YehZ is the putative periplasmic binding protein. Based on sequence similarity they probably function together as an ATP-dependant osmoprotection transporter. The yehX, yehW, yehY, and yehZ genes are located within a single operon. Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon, which was dependent upon σs |CITS:[15251200]|.)
GLYCAt2rpp "D-glycerate transport via proton symport, reversible ( periplasm )" glyc-R[p] + h[p] <==> glyc-R[c] + h[c] ( B3127 OR B2789 ) B2789 : (The YgcZ protein may function as a glucarate transporter. The ygcZ gene is encoded in a probable operon with genes encoding two subunits of a putative glucarate dehydratase. YgcZ is a member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]| and shares a high level of sequence similarity with probable glucarate transporters from various organisms. YgcZ probably functions as a glucarate/proton transporter.) B3127 : (YhaU is an uncharacterised member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]|. Based on sequence similarity, YhaU may function as a proton-driven glucarate uptake system.)
GLYCTO2 Glycolate oxidase [c] : glyclt + q8 --> glx + q8h2 ( B2979 AND B4467 AND B4468 ) B2979 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.) B4467 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.) B4468 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)
GLYCTO3 Glycolate oxidase [c] : glyclt + mqn8 --> glx + mql8 ( B2979 AND B4467 AND B4468 ) B2979 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.) B4467 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.) B4468 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)
GLYCTO4 Glycolate oxidase [c] : 2dmmq8 + glyclt --> 2dmmql8 + glx ( B2979 AND B4467 AND B4468 ) B2979 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.) B4467 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.) B4468 : (E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts; an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)
GUAtex Guanine transport via diffusion ( extracellular to periplasm ) gua[e] <==> gua[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
HEXt2rpp "hexanoate transport via proton symport, reversible ( periplasm )" h[p] + hxa[p] <==> h[c] + hxa[c] B2223 B2223 : (No information about this protein was found by a literature search conducted on June 13, 2005. )
HG2abcpp Mercury ( Hg+2 ) ABC transporter ( periplasm ) atp[c] + h2o[c] + hg2[c] --> adp[c] + h[c] + hg2[p] + pi[c] B3469 B3469 : (The gene product of the yhhO gene, also referred to as zntA, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|. ZntA displays a Km of approximately 20 μM for Cd(II) and 100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|. A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|. The zntA gene was found to be under the control of the transcriptional regulator ZntR. zntA expression is activated by an increased concentration of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by Zn(II) |CITS:[20127859]|.)
INOSTt4pp Na+/myo-inositol symporter ( periplasm ) inost[p] + na1[p] --> inost[c] + na1[c] B3679 B3679 : (The YidK protein is an uncharacterised member of the SSS superfamily of sodium dependent solute transporters |CITS: [94304911]|. Based on sequence similarity, YidK may function as a sodium-driven metabolite uptake system.)
INStex inosine transport via diffusion ( extracellular to periplasm ) ins[e] <==> ins[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
LYSt3pp L-lysine transport out via proton antiport ( cytoplasm to periplasm ) h[p] + lys-L[c] --> h[c] + lys-L[p] B2923 B2923 : (The ArgO (YggA) protein is a member of the LysE family of lysine efflux transporters |CITS: [99257453]|. Based on sequence similarity, ArgO may function as a proton-driven amino acid efflux system. Null mutations in both the argO and the argP genes cause hypersensitivity to canavanine, an arginine analog. ArgO expression is regulated by ArgP, and transcription of argO is induced by exogenous arginine |CITS: [15150242]|. ArgO = "arginine outward transport" |CITS: [15150242]|)
MMETt2pp S-methylmethionine permease ( periplasm ) h[p] + mmet[p] --> h[c] + mmet[c] B0260 B0260 : (MmuP belongs to the APC superfamily of amino acid transporters and is a putative S-methylmethionine transporter |CITS: [9882684]|. A mutant with a non-polar in-frame deletion in mmuP is unable to utilize S-methylmethionine as a source of methionine in a metE metH mutant background |CITS: [9882684]|. mmuP : "S-methylmethionine utilization" |CITS: [9882684]|)
MSO3abcpp methanesulfonate transport via ABC system ( periplasm ) atp[c] + h2o[c] + mso3[p] --> adp[c] + h[c] + mso3[c] + pi[c] ( B0936 AND B0933 AND B0934 ) B0933 : (Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.) B0934 : (Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.) B0936 : (Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)
NI2abcpp Nickle ( Ni+2 ) ABC transporter ( periplasm ) atp[c] + h2o[c] + ni2[c] --> adp[c] + h[c] + ni2[p] + pi[c] B3469 B3469 : (The gene product of the yhhO gene, also referred to as zntA, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|. ZntA displays a Km of approximately 20 μM for Cd(II) and 100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|. A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|. The zntA gene was found to be under the control of the transcriptional regulator ZntR. zntA expression is activated by an increased concentration of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by Zn(II) |CITS:[20127859]|.)
PPPNt2rpp "3-phenylpropionate transport via proton symport, reversible ( periplasm )" h[p] + pppn[p] <==> h[c] + pppn[c] B2536 B2536 : (HcaT is a member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]|. HcaT is a putative 3-phenylpropionate transporter. The hcaT gene is located immediately downstream of the hcaR gene, whose product regulates expression of the hcaA-D operon responsible for catabolism of 3-phenylpropionic acid |CITS: [98269008]|. Membrane topology predictions using experimentally determined C terminus locations indicate that HcaT has 12 transmembrane helices and the C-terminus is located in the cytoplasm |CITS:[15044727]|.)
PSCLYSt2pp psicoselysine transport via proton symport ( periplasm ) h[p] + psclys[p] --> h[c] + psclys[c] B3370 B3370 : (FrlA is an uncharacterized member of the APC superfamily of amino acid transporters |CITS:[20391827]|. Based on the activities of FrlB and FrlD, FrlA is suggested to transport fructoselysine, which can be utilized as a carbon source |CITS: [12147680]|. The function of FrlA has not been experimentally determined. An frlA mutant is unable to grow on 20mM fructoselysine or psicoselysine as the sole source of carbon |CITS: [14641112]|. FrlA: "fructoselysine" |CITS: [12147680]|.)
SULFACabcpp sulfoacetate transport via ABC system ( periplasm ) atp[c] + h2o[c] + sulfac[p] --> adp[c] + h[c] + pi[c] + sulfac[c] ( B0936 AND B0933 AND B0934 ) B0933 : (Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.) B0934 : (Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.) B0936 : (Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)
URItex uridine transport via diffusion ( extracellular to periplasm ) uri[e] <==> uri[p] B0411 B0411 : (Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli. It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]| It is believed to form a 14 strand β-barrel porin. The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)
XYLUt2pp L-xylulose transport in via proton symport ( periplasm ) h[p] + xylu-L[p] --> h[c] + xylu-L[c] ( B3577 AND B3578 AND B3579 ) B3577 : (Based on sequence similarity, the yiaMNO genes encode the only tri-partite ATP-independent periplasmic (TRAP) transporter in Escherichia coli. The TRAP transporters share characteristics of both the ATP-binding cassette (ABC) and secondary families of transporters |CITS:[11524131]|. Like the ABC transporters TRAP transporters use an extracytoplasmic solute-binding protein but rather than ATP hydrolysis the driving force is provided by either proton-(pmf) and/or sodium ion motive force (smf) |CITS:[11524131]|. Based on sequence similarity, YiaO is the periplasmic solute-binding protein and YiaM and YiaN are membrane-spanning proteins. Deletion mutation experiments |CITS:[14668138]| showed that deletion of the yiaMNO genes affected the ability of E.coli to utilize L-xylulose when growth was measured using various carbon substrates. Solute transport studies |CITS:[14668138]| determined that the yiaMNO deletion strain was capable of utilizing L-xylulose but at a lower rate, indicating that the YiaMNO transporter is involved in, but not essential for L-xylulose utilization. Purification and binding studies |CITS:[14668138]| using YiaO showed that YiaO was able to bind L-xylulose. Furthermore, spheroblasts expressing the YiaMN membrane domains were stimulated to increase uptake of L-xylulose when incubated with the periplasmic substrate-binding YiaO while those spheroblasts not expressing YiaMN showed no such stimulation. Deletion of yiaMNO resulted in a delay of entry into stationary phase of cells grown in LB with glucose, or minimal medium with glucose or other compounds. These cultures obtained a higher stationary phase OD660 and higher c.f.u. numbers. Deletion of yiaMNO also resulted in an increased lag time in cultures with high NaCl concentrations, and a reduction in biofilm formation in minimal medium with glucose |CITS:[15870475]|.) B3578 : (Based on sequence similarity, the yiaMNO genes encode the only tri-partite ATP-independent periplasmic (TRAP) transporter in Escherichia coli. The TRAP transporters share characteristics of both the ATP-binding cassette (ABC) and secondary families of transporters |CITS:[11524131]|. Like the ABC transporters TRAP transporters use an extracytoplasmic solute-binding protein but rather than ATP hydrolysis the driving force is provided by either proton-(pmf) and/or sodium ion motive force (smf) |CITS:[11524131]|. Based on sequence similarity, YiaO is the periplasmic solute-binding protein and YiaM and YiaN are membrane-spanning proteins. Deletion mutation experiments |CITS:[14668138]| showed that deletion of the yiaMNO genes affected the ability of E.coli to utilize L-xylulose when growth was measured using various carbon substrates. Solute transport studies |CITS:[14668138]| determined that the yiaMNO deletion strain was capable of utilizing L-xylulose but at a lower rate, indicating that the YiaMNO transporter is involved in, but not essential for L-xylulose utilization. Purification and binding studies |CITS:[14668138]| using YiaO showed that YiaO was able to bind L-xylulose. Furthermore, spheroblasts expressing the YiaMN membrane domains were stimulated to increase uptake of L-xylulose when incubated with the periplasmic substrate-binding YiaO while those spheroblasts not expressing YiaMN showed no such stimulation. Deletion of yiaMNO resulted in a delay of entry into stationary phase of cells grown in LB with glucose, or minimal medium with glucose or other compounds. These cultures obtained a higher stationary phase OD660 and higher c.f.u. numbers. Deletion of yiaMNO also resulted in an increased lag time in cultures with high NaCl concentrations, and a reduction in biofilm formation in minimal medium with glucose |CITS:[15870475]|.) B3579 : (Based on sequence similarity, the yiaMNO genes encode the only tri-partite ATP-independent periplasmic (TRAP) transporter in Escherichia coli. The TRAP transporters share characteristics of both the ATP-binding cassette (ABC) and secondary families of transporters |CITS:[11524131]|. Like the ABC transporters TRAP transporters use an extracytoplasmic solute-binding protein but rather than ATP hydrolysis the driving force is provided by either proton-(pmf) and/or sodium ion motive force (smf) |CITS:[11524131]|. Based on sequence similarity, YiaO is the periplasmic solute-binding protein and YiaM and YiaN are membrane-spanning proteins. Deletion mutation experiments |CITS:[14668138]| showed that deletion of the yiaMNO genes affected the ability of E.coli to utilize L-xylulose when growth was measured using various carbon substrates. Solute transport studies |CITS:[14668138]| determined that the yiaMNO deletion strain was capable of utilizing L-xylulose but at a lower rate, indicating that the YiaMNO transporter is involved in, but not essential for L-xylulose utilization. Purification and binding studies |CITS:[14668138]| using YiaO showed that YiaO was able to bind L-xylulose. Furthermore, spheroblasts expressing the YiaMN membrane domains were stimulated to increase uptake of L-xylulose when incubated with the periplasmic substrate-binding YiaO while those spheroblasts not expressing YiaMN showed no such stimulation. Deletion of yiaMNO resulted in a delay of entry into stationary phase of cells grown in LB with glucose, or minimal medium with glucose or other compounds. These cultures obtained a higher stationary phase OD660 and higher c.f.u. numbers. Deletion of yiaMNO also resulted in an increased lag time in cultures with high NaCl concentrations, and a reduction in biofilm formation in minimal medium with glucose |CITS:[15870475]|.)